Identification, characterization, and crystal structure of the omega class glutathione transferases

被引：584

作者：

Board, PG

Coggan, M

Chelvanayagam, G

Easteal, S

Jermiin, LS

Schulte, GK

Danley, DE

Hoth, LR

Griffor, MC

Kamath, AV

Rosner, MH

Chrunyk, BA

Perregaux, DE

Gabel, CA

Geoghegan, KF

Pandit, J

机构：

[1] Australian Natl Univ, John Curtin Sch Med Res, Mol Genet Grp, Canberra, ACT 2601, Australia

[2] Australian Natl Univ, John Curtin Sch Med Res, Human Genet Grp, Canberra, ACT 2601, Australia

[3] Univ Sydney, Australian Genom Informat Ctr, Sydney, NSW 2006, Australia

[4] Pfizer Global Res & Dev, Groton, CT 06340 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2000年 / 275卷 / 32期

关键词：

D O I：

10.1074/jbc.M001706200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment, Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans, In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins, The structure of GSTO 1-1 has been determined at 2.0-Angstrom resolution and has a characteristic GST fold (Protein Data Bank entry code leem). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione,

引用

页码：24798 / 24806

页数：9

共 61 条

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